-
1
-
-
77649202326
-
Protein aggregation diseases: Pathogenicity and therapeutic perspectives
-
Aguzzi, A.; O'Connor, T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat. Rev. Drug Discov., 2010, 9, 237-248.
-
(2010)
Nat. Rev. Drug Discov.
, vol.9
, pp. 237-248
-
-
Aguzzi, A.1
O'Connor, T.2
-
2
-
-
77952138141
-
Strategies for the inhibition of protein aggregation in human diseases
-
Bartolini, M.; Andrisano, V. Strategies for the inhibition of protein aggregation in human diseases. ChemBioChem, 2010, 11, 1018-1035.
-
(2010)
ChemBioChem
, vol.11
, pp. 1018-1035
-
-
Bartolini, M.1
Andrisano, V.2
-
3
-
-
77649240855
-
Identifying the amylome, proteins capable of forming amyloid-like fibrils
-
Goldschmidt, L.; Teng, P. K.; Riek, L.; Eisenberg, D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl. Acad. Sci. U. S. A., 2010, 107, 3487-3492.
-
(2010)
Proc. Natl. Acad. Sci. U. S. A.
, vol.107
, pp. 3487-3492
-
-
Goldschmidt, L.1
Teng, P.K.2
Riek, L.3
Eisenberg, D.4
-
4
-
-
23144459082
-
Molecular recycling within amyloid fibrils
-
DOI 10.1038/nature03986
-
Carulla, N.; Caddy, G. L.; Hall, D. R.; Zurdo, J.; Gairí, M.; Feliz, M.; Giralt, E.; Robinson, C. V.; Dobson, C. M. Molecular recycling within amyloid fibrils. Nature, 2005, 436, 554-558. (Pubitemid 41112928)
-
(2005)
Nature
, vol.436
, Issue.7050
, pp. 554-558
-
-
Carulla, N.1
Caddy, G.L.2
Hall, D.R.3
Zurdo, J.4
Gairi, M.5
Feliz, M.6
Giralt, E.7
Robinson, C.V.8
Dobson, C.M.9
-
5
-
-
33846160381
-
Polymorphism in the intermediates and products of amyloid assembly
-
DOI 10.1016/j.sbi.2007.01.007, PII S0959440X07000085, Foldinf and Binding / Protein-Nucleic Interactions
-
Kodali, R.; Wetzel, R. Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol, 2007, 17, 48-57. (Pubitemid 46242190)
-
(2007)
Current Opinion in Structural Biology
, vol.17
, Issue.1
, pp. 48-57
-
-
Kodali, R.1
Wetzel, R.2
-
6
-
-
33846054061
-
Disrupting-amyloid aggregation for Alzheimer disease treatment
-
DOI 10.2174/156802607779318262
-
Estrada, L. D.; Soto, C. Disrupting p-amyloid aggregation for Alzheimer's disease treatment. Curr. Top. Med. Chem., 2007, 7, 115-126. (Pubitemid 46062400)
-
(2007)
Current Topics in Medicinal Chemistry
, vol.7
, Issue.1
, pp. 115-126
-
-
Estrada, L.D.1
Soto, C.2
-
7
-
-
44949181936
-
Amyloids: Friend or foe?
-
Hammer, N. D.; Wang, X.; McGuffie, B. A.; Chapman, M. R. Amyloids: friend or foe? J. Alzheimer Dis., 2008, 13, 407-419. (Pubitemid 352039020)
-
(2008)
Journal of Alzheimer's Disease
, vol.13
, Issue.4
, pp. 407-419
-
-
Hammer, N.D.1
Wang, X.2
McGuffie, B.A.3
Chapman, M.R.4
-
8
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
DOI 10.1146/annurev.biochem.75.101304.123901
-
Chiti, F.; Dobson, CM. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem., 2006, 75, 333-366. (Pubitemid 44118036)
-
(2006)
Annual Review of Biochemistry
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
9
-
-
0025753852
-
The molecular pathology of Alzheimer's disease
-
Selkoe, DJ. The molecular pathology of Alzheimer's disease. Neuron, 1991, 6, 487-498.
-
(1991)
Neuron
, vol.6
, pp. 487-498
-
-
Selkoe, D.J.1
-
10
-
-
0026597063
-
Alzheimer's disease: The amyloid cascade hypothesis
-
Hardy, J. A.; Higgins, G. A. Alzheimer's disease: the amyloid cascade hypothesis. Science, 1992, 256, 184-185.
-
(1992)
Science
, vol.256
, pp. 184-185
-
-
Hardy, J.A.1
Higgins, G.A.2
-
11
-
-
0037135111
-
The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
-
DOI 10.1126/science.1072994
-
Hardy, J.; Selkoe, DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science, 2002, 297, 353-356. (Pubitemid 34790756)
-
(2002)
Science
, vol.297
, Issue.5580
, pp. 353-356
-
-
Hardy, J.1
Selkoe, D.J.2
-
12
-
-
60349125886
-
Reassessing the amyloid cascade hypothesis of Alzheimer's disease
-
Pimplikar, S. W. Reassessing the amyloid cascade hypothesis of Alzheimer's disease. Int. J. Biochem. Cell Biol, 2009, 41, 1261-1268.
-
(2009)
Int. J. Biochem. Cell Biol
, vol.41
, pp. 1261-1268
-
-
Pimplikar, S.W.1
-
13
-
-
64349107868
-
Small molecule inhibitors of Ap aggregation and neurotoxicity
-
Hawkes, C. A.; Ng, V.; McLaurin, J. Small molecule inhibitors of Ap aggregation and neurotoxicity. Drug Dev. Res., 2009, 70, 111-124.
-
(2009)
Drug Dev. Res.
, vol.70
, pp. 111-124
-
-
Hawkes, C.A.1
Ng, V.2
McLaurin, J.3
-
14
-
-
77955639372
-
Beta amyloid aggregation inhibitors: Small molecules as candidate drugs for therapy of Alzheimer's disease
-
Re, F.; Airoldi, C; Zona, C; Masserini, M.; La Ferla, B.; Quattrocchi, N.; Nicotra, F. Beta amyloid aggregation inhibitors: small molecules as candidate drugs for therapy of Alzheimer's disease. Curr. Med. Chem., 2010, 17, 2990-3006.
-
(2010)
Curr. Med. Chem.
, vol.17
, pp. 2990-3006
-
-
Re, F.1
Airoldi, C.2
Zona, C.3
Masserini, M.4
La Ferla, B.5
Quattrocchi, N.6
Nicotra, F.7
-
15
-
-
84864544333
-
Metal compounds as inhibitors of p-amyloid aggregation. Perspectives for an innovative metallotherapeutics on Alzheimer's disease
-
Valensin, D.; Gabbiani, C; Messori, L. Metal compounds as inhibitors of p-amyloid aggregation. Perspectives for an innovative metallotherapeutics on Alzheimer's disease. Coord. Chem. Rev., 2012, 256, 2357-2366.
-
(2012)
Coord. Chem. Rev.
, vol.256
, pp. 2357-2366
-
-
Valensin, D.1
Gabbiani, C.2
Messori, L.3
-
16
-
-
84867477898
-
The amyloid beta peptide: A chemist's perspective. Role in Alzheimer's and fibrillization
-
The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization. Chem. Rev., 2012, 112, 5147-5192.
-
(2012)
Chem. Rev.
, vol.112
, pp. 5147-5192
-
-
-
17
-
-
84862806815
-
Pharmacotherapies for Alzheimer's disease: Beyond cholinesterase inhibitors
-
Tayeb, H. O.; Yang, H. D.; Price, B. H.; Tarazi, F. I. Pharmacotherapies for Alzheimer's disease: beyond cholinesterase inhibitors. Pharmacol. Ther., 2012, 134, 8-25.
-
(2012)
Pharmacol. Ther.
, vol.134
, pp. 8-25
-
-
Tayeb, H.O.1
Yang, H.D.2
Price, B.H.3
Tarazi, F.I.4
-
18
-
-
0027502784
-
Thioflavine T interaction with synthetic Alzheimer's disease-amyloid peptides: Detection of amyloid aggregation in solution
-
Le Vine, H., III. Thioflavine T interaction with synthetic Alzheimer's disease/J-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci., 1993, 2, 404-410. (Pubitemid 23071288)
-
(1993)
Protein Science
, vol.2
, Issue.3
, pp. 404-410
-
-
LeVine III, H.1
-
19
-
-
0037298750
-
Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies
-
DOI 10.1016/S0006-2952(02)01514-9, PII S0006295202015149
-
Bartolini, M.; Bertucci, C; Cavrini, V.; Andrisano, V. p-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies. Biochem. Pharmacol, 2003, 65, 407-416. (Pubitemid 36084557)
-
(2003)
Biochemical Pharmacology
, vol.65
, Issue.3
, pp. 407-416
-
-
Bartolini, M.1
Bertucci, C.2
Cavrini, V.3
Andrisano, V.4
-
20
-
-
36849078628
-
Insight into the kinetic of amyloid (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
-
DOI 10.1002/cbic.200700427
-
Bartolini, M.; Bertucci, C; Bolognesi, M. L.; Cavalli, A.; Melchiorre, C; Andrisano, V. Insight into the kinetic of amyloid/J (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action. ChemBioChem, 2007, 8, 2152-2161. (Pubitemid 350220767)
-
(2007)
ChemBioChem
, vol.8
, Issue.17
, pp. 2152-2161
-
-
Bartolini, M.1
Bertucci, C.2
Bolognesi, M.L.3
Cavalli, A.4
Melchiorre, C.5
Andrisano, V.6
-
21
-
-
52049102256
-
Structural requirements for the flavonoid fisetin in inhibiting fibril formation of amyloid beta protein
-
Akaishi, T.; Morimoto, T.; Shibao, M.; Watanabe, S.; Sakai-Kato, K.; Utsunomiya-Tate, N.; Abe, K. Structural requirements for the flavonoid fisetin in inhibiting fibril formation of amyloid beta protein. Neurosci. Lett., 2008, 444, 280-285.
-
(2008)
Neurosci. Lett.
, vol.444
, pp. 280-285
-
-
Akaishi, T.1
Morimoto, T.2
Shibao, M.3
Watanabe, S.4
Sakai-Kato, K.5
Utsunomiya-Tate, N.6
Abe, K.7
-
22
-
-
84874098413
-
Sym-Triazines for directed multitarget modulation of cholinesterases and amyloid-p in Alzheimer's disease
-
Veloso, A. J.; Dhar, D.; Chow, A. M.; Zhang, B.; Tang, D. W. F.; Ganesh, H. V. S.; Mikhaylichenko, S.; Brown, I. R.; Kerman, K. sym-Triazines for directed multitarget modulation of cholinesterases and amyloid-p in Alzheimer's disease. ACS Chem. Neurosci., 2013, 4, 339-349.
-
(2013)
ACS Chem. Neurosci.
, vol.4
, pp. 339-349
-
-
Veloso, A.J.1
Dhar, D.2
Chow, A.M.3
Zhang, B.4
Tang, D.W.F.5
Ganesh, H.V.S.6
Mikhaylichenko, S.7
Brown, I.R.8
Kerman, K.9
-
23
-
-
0742305866
-
Network biology: Understanding the cell's functional organization
-
DOI 10.1038/nrg1272
-
Barabási, A. L.; Oltvai, Z. N.; Network biology: understanding the cell's functional organization. Nat. Rev. Genet., 2004, 5, 101-113. (Pubitemid 38160277)
-
(2004)
Nature Reviews Genetics
, vol.5
, Issue.2
, pp. 101-113
-
-
Barabasi, A.-L.1
Oltvai, Z.N.2
-
24
-
-
84877947846
-
Human disease and drug pharmacology, complex as real life
-
Viayna, E.; Sola, I.; Di Pietro, O.; Muñoz-Torrero, D. Human disease and drug pharmacology, complex as real life. Curr. Med. Chem., 2013, 20, 1623-1634.
-
(2013)
Curr. Med. Chem.
, vol.20
, pp. 1623-1634
-
-
Viayna, E.1
Sola, I.2
Di Pietro, O.3
Muñoz-Torrero, D.4
-
25
-
-
84861490509
-
Modern phenotypic drug discovery is a viable, neoclassic pharma strategy
-
Lee, J. A.; Uhlik, M. T.; Moxham, CM.; Tomandl, D.; Sall, DJ. Modern phenotypic drug discovery is a viable, neoclassic pharma strategy. J. Med. Chem., 2012, 55, 4527-4538.
-
(2012)
J. Med. Chem.
, vol.55
, pp. 4527-4538
-
-
Lee, J.A.1
Uhlik, M.T.2
Moxham, C.M.3
Tomandl, D.4
Sall, D.J.5
-
26
-
-
0041822089
-
Join the crowd
-
DOI 10.1038/425027a
-
Ellis, R. J.; Minton, A. P. Join the crowd. Nature, 2003, 425, 27-28. (Pubitemid 37101701)
-
(2003)
Nature
, vol.425
, Issue.6953
, pp. 27-28
-
-
Ellis, R.J.1
Minton, A.P.2
-
27
-
-
84873744026
-
Why and how protein aggregation has to be studied in vivo
-
Ami, D.; Natalello, A.; Lotti, M.; Doglia, S. M. Why and how protein aggregation has to be studied in vivo. Microb. Cell Fact., 2013, 12, 17.
-
(2013)
Microb. Cell Fact.
, vol.12
, pp. 17
-
-
Ami, D.1
Natalello, A.2
Lotti, M.3
Doglia, S.M.4
-
29
-
-
33646106328
-
Protein quality in bacterial inclusion bodies
-
Ventura, S.; Villaverde, A. Protein quality in bacterial inclusion bodies. Trends Biotechnol, 2006, 24, 179-185.
-
(2006)
Trends Biotechnol
, vol.24
, pp. 179-185
-
-
Ventura, S.1
Villaverde, A.2
-
30
-
-
68249086335
-
Amyloids in bacterial inclusion bodies
-
de Groot, N. S.; Sabate, R.; Ventura, S. Amyloids in bacterial inclusion bodies. Trends Biochem. Sci., 2009, 34, 408-416.
-
(2009)
Trends Biochem. Sci.
, vol.34
, pp. 408-416
-
-
De Groot, N.S.1
Sabate, R.2
Ventura, S.3
-
31
-
-
50249144570
-
Bacterial inclusion bodies contain amyloid-like structure
-
Wang, L.; Maji, S. K.; Sawaya, M. R.; Eisenberg, D.; Riek, R. Bacterial inclusion bodies contain amyloid-like structure. PLoS Biol, 2008, 6, e195.
-
(2008)
PLoS Biol
, vol.6
-
-
Wang, L.1
Maji, S.K.2
Sawaya, M.R.3
Eisenberg, D.4
Riek, R.5
-
32
-
-
79551595773
-
Bacterial inclusion bodies of Alzheimer's disease (3-amyloid peptides can be employed to study native-like aggregation intermediate states
-
Dasari, M.; Espargaro, A.; Sabate, R.; Lopez del Amo, J. M.; Fink, U.; Grelle, G.; Bieschke, J.; Ventura, S.; Reif, B. Bacterial inclusion bodies of Alzheimer's disease (3-amyloid peptides can be employed to study native-like aggregation intermediate states. ChemBioChem, 2011, 12, 407-423.
-
(2011)
ChemBioChem
, vol.12
, pp. 407-423
-
-
Dasari, M.1
Espargaro, A.2
Sabate, R.3
Lopez Del Amo, J.M.4
Fink, U.5
Grelle, G.6
Bieschke, J.7
Ventura, S.8
Reif, B.9
-
33
-
-
15244362270
-
Amyloid-like properties of bacterial inclusion bodies
-
DOI 10.1016/j.jmb.2005.02.030
-
Carrió, M.; González-Montalbán, N.; Vera, A.; Villaverde, A.; Ventura, S. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol, 2005, 347, 1025-1037. (Pubitemid 40387450)
-
(2005)
Journal of Molecular Biology
, vol.347
, Issue.5
, pp. 1025-1037
-
-
Carrio, M.1
Gonzalez-Montalban, N.2
Vera, A.3
Villaverde, A.4
Ventura, S.5
-
34
-
-
84860363205
-
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
-
Villar-Piqué, A.; Espargaró, A.; Sabaté, R.; de Groot, N. S.; Ventura, S. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microb. Cell Fact., 2012, 11, 55.
-
(2012)
Microb. Cell Fact.
, vol.11
, pp. 55
-
-
Villar-Piqué, A.1
Espargaró, A.2
Sabaté, R.3
De Groot, N.S.4
Ventura, S.5
-
35
-
-
84867350646
-
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation
-
Espargaró, A.; Sabate, R.; Ventura, S. Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation. Mol. Biosyst., 2012, 8, 2839-2844.
-
(2012)
Mol. Biosyst.
, vol.8
, pp. 2839-2844
-
-
Espargaró, A.1
Sabate, R.2
Ventura, S.3
-
36
-
-
36348954399
-
The use of rigid, fibrillar Congo red nanostructures for scaffolding protein assemblies and inducing the formation of amyloid-like arrangement of molecules
-
DOI 10.1111/j.1747-0285.2007.00589.x
-
Spólnik, P.; Stopa, B.; Piekarska, B.; Jagusiak, A.; Konieczny, L.; Rybarska, J.; Król, M.; Roterman, I.; Urbanowicz, B.; Zieba-Palus, J. The use of rigid, fibrillar Congo red nanostructures for scaffolding protein assemblies and inducing the formation of amyloid-like arrangement of molecules. Chem. Biol. Drug Des., 2007, 70, 491-501. (Pubitemid 350150871)
-
(2007)
Chemical Biology and Drug Design
, vol.70
, Issue.6
, pp. 491-501
-
-
Spolnik, P.1
Stopa, B.2
Piekarska, B.3
Jagusiak, A.4
Konieczny, L.5
Rybarska, J.6
Krol, M.7
Roterman, I.8
Urbanowicz, B.9
Zieba-Palus, J.10
-
37
-
-
33645115011
-
Mechanism of thioflavin T accumulation inside cells overexpressing P-glycoprotein or multidrug resistance-associated protein: Role of lipophilicity and positive charge
-
Darghal, N.; Garnier-Suillerot, A.; Salerno, M. Mechanism of thioflavin T accumulation inside cells overexpressing P-glycoprotein or multidrug resistance-associated protein: role of lipophilicity and positive charge. Biochem. Biophys. Res. Commun., 2006, 343, 623-629.
-
(2006)
Biochem. Biophys. Res. Commun.
, vol.343
, pp. 623-629
-
-
Darghal, N.1
Garnier-Suillerot, A.2
Salerno, M.3
-
38
-
-
0032849874
-
Quantification of-sheet amyloid fibril structures with thioflavin T
-
DOI 10.1016/S0076-6879(99)09020-5
-
Le Vine, H., III. Quantification of (3-sheet amyloid fibril structures with thioflavin T. Methods Enzymol, 1999, 309, 274-284. (Pubitemid 29446455)
-
(1999)
Methods in Enzymology
, vol.309
, pp. 274-284
-
-
LeVine III, H.1
-
39
-
-
0035349804
-
Inhibition of Alzheimer's disease (3-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy
-
De Felice, F. G.; Houzel, J.-C; Garcia-Abreu, J.; Louzada, P. R. F., Jr.; Afonso, R. C.; Meirelles, M. N. L.; Lent, R.; Neto, V. M.; Ferreira, S. T. Inhibition of Alzheimer's disease (3-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy. FASEB J., 2001, 15, 1297-1299.
-
(2001)
FASEB J.
, vol.15
, pp. 1297-1299
-
-
De Felice, F.G.1
Houzel, J.-C.2
Garcia-Abreu, J.3
Louzada Jr., P.R.F.4
Afonso, R.C.5
Meirelles, M.N.L.6
Lent, R.7
Neto, V.M.8
Ferreira, S.T.9
-
40
-
-
0037195163
-
Neurotoxic effects of thioflavin S-positive amyloid deposits in transgenic mice and Alzheimer's disease
-
DOI 10.1073/pnas.222433299
-
Urbanc, B.; Cruz, L.; Le, R.; Sanders, J.; Hsiao Ashe, K.; Duff, K.; Stanley, H. E.; Irizarry, M. C.; Hyman, B. T. Neurotoxic effects of thioflavin S-positive amyloid deposits in transgenic mice and Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A., 2002, 99, 13990-13995. (Pubitemid 35257612)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.22
, pp. 13990-13995
-
-
Urbanc, B.1
Cruz, L.2
Le, R.3
Sanders, J.4
Hsiao Ashe, K.5
Duff, K.6
Stanley, H.E.7
Irizarry, M.C.8
Hyman, B.T.9
-
41
-
-
0034736034
-
New tacrine-huperzine A hybrids (huprines): Highly potent tight-binding acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease
-
Camps, P.; El Achab, R.; Morral, J.; Muñoz-Torrero, D.; Badia, A.; Baños, J. E.; Vivas, N. M.; Barril, X.; Orozco, M.; Luque, FJ. New tacrine-huperzine A hybrids (huprines): highly potent tight-binding acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease. J. Med. Chem., 2000, 43, 4657-4666.
-
(2000)
J. Med. Chem.
, vol.43
, pp. 4657-4666
-
-
Camps, P.1
El Achab, R.2
Morral, J.3
Muñoz-Torrero, D.4
Badia, A.5
Baños, J.E.6
Vivas, N.M.7
Barril, X.8
Orozco, M.9
Luque, F.J.10
-
42
-
-
69949089936
-
Pyrano[3, 2-c]quinoline-6-chlorotacrine hybrids as a novel family of acetylcholinesterase-and/J-amyloid-directed anti-Alzheimer compounds
-
Camps, P.; Formosa, X.; Galdeano, C; Muñoz-Torrero, D.; Ramírez, L.; Gómez, E.; Isambert, N.; Lavilla, R.; Badia, A.; Clos, M. V.; Bartolini, M.; Mancini, F.; Andrisano, V.; Arce, M. P.; Rodríguez-Franco, M. I.; Huertas, O.; Dafni, T.; Luque, FJ. Pyrano[3, 2-c]quinoline-6-chlorotacrine hybrids as a novel family of acetylcholinesterase- and/J-amyloid-directed anti-Alzheimer compounds. J. Med. Chem., 2009, 52, 5365-5379.
-
(2009)
J. Med. Chem.
, vol.52
, pp. 5365-5379
-
-
Camps, P.1
Formosa, X.2
Galdeano, C.3
Muñoz-Torrero, D.4
Ramírez, L.5
Gómez, E.6
Isambert, N.7
Lavilla, R.8
Badia, A.9
Clos, M.V.10
Bartolini, M.11
Mancini, F.12
Andrisano, V.13
Arce, M.P.14
Rodríguez-Franco, M.I.15
Huertas, O.16
Dafni, T.17
Luque, F.J.18
-
43
-
-
84856378492
-
Huprine-tacrine heterodimers as antiamyloidogenic compounds of potential interest against Alzheimer's and prion diseases
-
Galdeano, C; Viayna, E.; Sola, I.; Formosa, X.; Camps, P.; Badia, A.; Clos, M. V.; Relat, J.; Ratia, M.; Bartolini, M.; Mancini, F.; Andrisano, V.; Salmona, M.; Minguillón, C; González-Muñoz, G. C.; Rodríguez-Franco, M. I.; Bidon-Chanal, A.; Luque, FJ.; Muñoz-Torrero, D. Huprine-tacrine heterodimers as antiamyloidogenic compounds of potential interest against Alzheimer's and prion diseases. J. Med. Chem., 2012, 55, 661-669.
-
(2012)
J. Med. Chem.
, vol.55
, pp. 661-669
-
-
Galdeano, C.1
Viayna, E.2
Sola, I.3
Formosa, X.4
Camps, P.5
Badia, A.6
Clos, M.V.7
Relat, J.8
Ratia, M.9
Bartolini, M.10
Mancini, F.11
Andrisano, V.12
Salmona, M.13
Minguillón, C.14
González-Muñoz, G.C.15
Rodríguez-Franco, M.I.16
Bidon-Chanal, A.17
Luque, F.J.18
Muñoz-Torrero, D.19
-
44
-
-
78349232410
-
Novel huprine derivatives with inhibitory activity toward (3-amyloid aggregation and formation as diseasemodifying anti-Alzheimer drug candidates
-
Viayna, E.; Gómez, T.; Galdeano, C; Ramírez, L.; Ratia, M.; Badia, A.; Clos, M. V.; Verdaguer, E.; Junyent, F.; Camins, A.; Pallàs, M.; Bartolini, M.; Mancini, F.; Andrisano, V.; Arce, M. P.; Rodríguez- Franco, M. I.; Bidon-Chanal, A.; Luque, FJ.; Camps, P.; Muñoz-Torrero, D. Novel huprine derivatives with inhibitory activity toward (3-amyloid aggregation and formation as diseasemodifying anti-Alzheimer drug candidates. ChemMedChem, 2010, 5, 1855-1870.
-
(2010)
ChemMedChem
, vol.5
, pp. 1855-1870
-
-
Viayna, E.1
Gómez, T.2
Galdeano, C.3
Ramírez, L.4
Ratia, M.5
Badia, A.6
Clos, M.V.7
Verdaguer, E.8
Junyent, F.9
Camins, A.10
Pallàs, M.11
Bartolini, M.12
Mancini, F.13
Andrisano, V.14
Arce, M.P.15
Rodríguez-Franco, M.I.16
Bidon-Chanal, A.17
Luque, F.J.18
Camps, P.19
Muñoz-Torrero, D.20
more..
-
45
-
-
0037359940
-
Disaggregating effects of ethanol at low concentration on-poly-L-lysines
-
DOI 10.1016/S0141-8130(03)00019-9
-
Sabaté, R.; Estelrich, J. Disaggregating effects of ethanol at low concentration on beta-poly-L-lysines. Int. J. Biol. Macromol, 2003, 32, 10-16. (Pubitemid 36444513)
-
(2003)
International Journal of Biological Macromolecules
, vol.32
, Issue.1-2
, pp. 10-16
-
-
Sabate, R.1
Estelrich, J.2
-
46
-
-
0036091892
-
Effect of diethylsulphoxide on growth, survival and ion exchange of Escherichia coli
-
DOI 10.1046/j.1472-765X.2002.01112.x
-
Markarian, S. A.; Poladyan, A. A.; Kirakosyan, G. R.; Trchounian, A. A.; Bagramyan, K. A. Effect of diethylsulphoxide on growth, survival and ion exchange of Escherichia coli. Lett. Appl. Microbiol, 2002, 34, 417-421. (Pubitemid 34534229)
-
(2002)
Letters in Applied Microbiology
, vol.34
, Issue.6
, pp. 417-421
-
-
Markarian, S.A.1
Poladyan, A.A.2
Kirakosyan, G.R.3
Trchounian, A.A.4
Bagramyan, K.A.5
-
47
-
-
78951490605
-
Effect of various solvents on bacterial growth in context of determining MIC of various antimicrobials
-
DOI: 10.5580/b43
-
Wadhwani, T.; Desai, K.; Patel, D.; Lawani, D.; Bahaley, P.; Joshi, P.; Kothari, V. Effect of various solvents on bacterial growth in context of determining MIC of various antimicrobials. Internet J. Microbiol, 2009, 7 (1). DOI: 10.5580/b43.
-
(2009)
Internet J. Microbiol
, vol.7
, Issue.1
-
-
Wadhwani, T.1
Desai, K.2
Patel, D.3
Lawani, D.4
Bahaley, P.5
Joshi, P.6
Kothari, V.7
-
48
-
-
0038219626
-
Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
-
DOI 10.1093/emboj/cdg213
-
Balguerie, A.; Dos Reis, S.; Ritter, C; Chaignepain, S.; Coulary-Salin, B.; Forge, V.; Bathany, K.; Lascu, I.; Schmitter, J.-M.; Riek, L.; Saupe, SJ. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J., 2003, 22, 2071-2081. (Pubitemid 36565532)
-
(2003)
EMBO Journal
, vol.22
, Issue.9
, pp. 2071-2081
-
-
Balguerie, A.1
Dos Reis, S.2
Ritter, C.3
Chaignepain, S.4
Coulary-Salin, B.5
Forge, V.6
Bathany, K.7
Lascu, I.8
Schmitter, J.-M.9
Riek, R.10
Saupe, S.J.11
-
49
-
-
34948904272
-
Novel class of quinone-bearing polyamines as multi-target-directed ligands to combat Alzheimer's disease
-
DOI 10.1021/jm070559a
-
Bolognesi, M. L.; Banzi, R.; Bartolini, M.; Cavalli, A.; Tarozzi, A.; Andrisano, V.; Minarini, A.; Rosini, M.; Tumiatti, V.; Bergamini, C; Fato, R.; Lenaz, G.; Hrelia, P.; Cattaneo, A.; Recanatini, M.; Melchiorre, C. Novel class of quinone-bearing polyamines as multi-target-directed ligands to combat Alzheimer's disease. J. Med. Chem., 2007, 50, 4882-4897. (Pubitemid 47525472)
-
(2007)
Journal of Medicinal Chemistry
, vol.50
, Issue.20
, pp. 4882-4897
-
-
Bolognesi, M.L.1
Banzi, R.2
Bartolini, M.3
Cavalli, A.4
Tarozzi, A.5
Andrisano, V.6
Minarini, A.7
Rosini, M.8
Tumiatti, V.9
Bergamini, C.10
Fato, R.11
Lenaz, G.12
Hrelia, P.13
Cattaneo, A.14
Recanatini, M.15
Melchiorre, C.16
-
50
-
-
34249860495
-
Small molecule inhibitors of aggregation indicate that amyloid oligomerization and fibrillization pathways are independent and distinct
-
DOI 10.1074/jbc.M608207200
-
Necula, M.; Kayed, R.; Milton, S.; Glabe, C. G. Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem., 2007, 282, 10311-10324. (Pubitemid 47093410)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.14
, pp. 10311-10324
-
-
Necula, M.1
Kayed, R.2
Milton, S.3
Glabe, C.G.4
-
51
-
-
33750739260
-
Same causes, same cures
-
DOI 10.1016/j.bbrc.2006.10.086, PII S0006291X06023552
-
Zhang, H.-Y. Same causes, same cures. Biochem. Biophys. Res. Commun., 2006, 351, 578-581. (Pubitemid 44708866)
-
(2006)
Biochemical and Biophysical Research Communications
, vol.351
, Issue.3
, pp. 578-581
-
-
Zhang, H.-Y.1
-
52
-
-
33745991934
-
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
-
DOI 10.1016/j.jbiotec.2006.02.026, PII S0168165606002070
-
de Groot, N. S.; Ventura, S. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J. Biotechnol, 2006, 125, 110-113. (Pubitemid 44066612)
-
(2006)
Journal of Biotechnology
, vol.125
, Issue.1
, pp. 110-113
-
-
De Groot, N.S.1
Ventura, S.2
-
53
-
-
42649110014
-
The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: The SH3 case
-
Espargaro, A.; Castillo, V.; de Groot, N. S.; Ventura, S. The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. J. Mol. Biol, 2008, 378, 1116-1131.
-
(2008)
J. Mol. Biol
, vol.378
, pp. 1116-1131
-
-
Espargaro, A.1
Castillo, V.2
De Groot, N.S.3
Ventura, S.4
-
54
-
-
15444373859
-
Investigating the effects of mutations on protein aggregation in the cell
-
DOI 10.1074/jbc.M412951200
-
Calloni, G.; Zoffoli, S.; Stefani, M.; Dobson, CM.; Chiti, F. Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem., 2005, 280, 10607-10613. (Pubitemid 40395922)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.11
, pp. 10607-10613
-
-
Calloni, G.1
Zoffoli, S.2
Stefani, M.3
Dobson, C.M.4
Chiti, F.5
-
55
-
-
34547687667
-
Correlation of Levels of Folded Recombinant p53 in Escherichia coli with Thermodynamic Stability in Vitro
-
DOI 10.1016/j.jmb.2007.06.044, PII S002228360700839X
-
Mayer, S.; Rudiger, S.; Ang, H. C.; Joerger, A. C.; Fersht, A. R. Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro. J. Mol. Biol, 2007, 372, 268-276. (Pubitemid 47223226)
-
(2007)
Journal of Molecular Biology
, vol.372
, Issue.1
, pp. 268-276
-
-
Mayer, S.1
Rudiger, S.2
Ang, H.C.3
Joerger, A.C.4
Fersht, A.R.5
-
56
-
-
33750449952
-
A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide
-
Kim, W.; Kim, Y.; Min, J.; Kim, D. J.; Chang, Y. T.; Hecht, M. H. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem. Biol, 2006, 1, 461-469.
-
(2006)
ACS Chem. Biol
, vol.1
, pp. 461-469
-
-
Kim, W.1
Kim, Y.2
Min, J.3
Kim, D.J.4
Chang, Y.T.5
Hecht, M.H.6
-
57
-
-
84866640341
-
Physicochemical strategies for inhibition of amyloid fibril formation: An overview of recent advances
-
Liu, R.; Su, R.; Liang, M.; Huang, R.; Wang, M.; Qi, W.; He, Z. Physicochemical strategies for inhibition of amyloid fibril formation: an overview of recent advances. Curr. Med. Chem., 2012, 19, 4157-4174.
-
(2012)
Curr. Med. Chem.
, vol.19
, pp. 4157-4174
-
-
Liu, R.1
Su, R.2
Liang, M.3
Huang, R.4
Wang, M.5
Qi, W.6
He, Z.7
-
58
-
-
84860521452
-
Role of ligand-based drug design methodologies toward the discovery of new anti-Alzheimer agents: Futures perspectives in fragment-based ligand design
-
Speck-Planche, A.; Luan, F.; Cordeiro, M. N. Role of ligand-based drug design methodologies toward the discovery of new anti-Alzheimer agents: futures perspectives in fragment-based ligand design. Curr. Med. Chem., 2012, 19, 1635-1645.
-
(2012)
Curr. Med. Chem.
, vol.19
, pp. 1635-1645
-
-
Speck-Planche, A.1
Luan, F.2
Cordeiro, M.N.3
|